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The 2019 coronavirus (SARS-CoV-2) surface protein (Spike) S1 Receptor Binding Domain undergoes conformational change upon heparin binding

Courtney Mycroft-West, View ORCID ProfileDunhao Su, View ORCID ProfileStefano Elli, View ORCID ProfileScott Guimond, View ORCID ProfileGavin Miller, View ORCID ProfileJeremy Turnbull, View ORCID ProfileEdwin Yates, View ORCID ProfileMarco Guerrini, View ORCID ProfileDavid Fernig, View ORCID ProfileMarcelo Lima, View ORCID ProfileMark Skidmore
doi: https://doi.org/10.1101/2020.02.29.971093
Courtney Mycroft-West
1Molecular & Structural Biosciences, School of Life Sciences, Keele University, Newcastle-Under-Lyme, Staffordshire, ST5 5BG, United Kingdom
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Dunhao Su
2Department of Biochemistry, Institute of Integrative Biology, University of Liverpool, Crown Street, Liverpool, L69 7ZB, United Kingdom
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Stefano Elli
3Istituto di Ricerche Chimiche e Biochimiche G. Ronzoni, Via G. Colombo 81, 20133, Milan, Italy
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Scott Guimond
4School of Medicine, Keele University, Newcastle-Under-Lyme, Staffordshire, ST5 5BG, United Kingdom
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Gavin Miller
5School of Chemistry, Keele University, Newcastle-Under-Lyme, Staffordshire, ST5 5BG, United Kingdom
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Jeremy Turnbull
2Department of Biochemistry, Institute of Integrative Biology, University of Liverpool, Crown Street, Liverpool, L69 7ZB, United Kingdom
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Edwin Yates
2Department of Biochemistry, Institute of Integrative Biology, University of Liverpool, Crown Street, Liverpool, L69 7ZB, United Kingdom
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Marco Guerrini
3Istituto di Ricerche Chimiche e Biochimiche G. Ronzoni, Via G. Colombo 81, 20133, Milan, Italy
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David Fernig
2Department of Biochemistry, Institute of Integrative Biology, University of Liverpool, Crown Street, Liverpool, L69 7ZB, United Kingdom
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Marcelo Lima
1Molecular & Structural Biosciences, School of Life Sciences, Keele University, Newcastle-Under-Lyme, Staffordshire, ST5 5BG, United Kingdom
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Mark Skidmore
1Molecular & Structural Biosciences, School of Life Sciences, Keele University, Newcastle-Under-Lyme, Staffordshire, ST5 5BG, United Kingdom
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  • For correspondence: m.a.skidmore@keele.ac.uk
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Abstract

Many pathogens take advantage of the dependence of the host on the interaction of hundreds of extracellular proteins with the glycosaminoglycans heparan sulfate to regulate homeostasis and use heparan sulfate as a means to adhere and gain access to cells. Moreover, mucosal epithelia such as that of the respiratory tract are protected by a layer of mucin polysaccharides, which are usually sulfated. Consequently, the polydisperse, natural products of heparan sulfate and the allied polysaccharide, heparin have been found to be involved and prevent infection by a range of viruses including S-associated coronavirus strain HSR1. Here we use surface plasmon resonance and circular dichroism to measure the interaction between the SARS-CoV-2 Spike S1 protein receptor binding domain (SARS-CoV-2 S1 RBD) and heparin. The data demonstrate an interaction between the recombinant surface receptor binding domain and the polysaccharide. This has implications for the rapid development of a first-line therapeutic by repurposing heparin and for next-generation, tailor-made, GAG-based antivirals.

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Posted March 02, 2020.
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The 2019 coronavirus (SARS-CoV-2) surface protein (Spike) S1 Receptor Binding Domain undergoes conformational change upon heparin binding
Courtney Mycroft-West, Dunhao Su, Stefano Elli, Scott Guimond, Gavin Miller, Jeremy Turnbull, Edwin Yates, Marco Guerrini, David Fernig, Marcelo Lima, Mark Skidmore
bioRxiv 2020.02.29.971093; doi: https://doi.org/10.1101/2020.02.29.971093
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The 2019 coronavirus (SARS-CoV-2) surface protein (Spike) S1 Receptor Binding Domain undergoes conformational change upon heparin binding
Courtney Mycroft-West, Dunhao Su, Stefano Elli, Scott Guimond, Gavin Miller, Jeremy Turnbull, Edwin Yates, Marco Guerrini, David Fernig, Marcelo Lima, Mark Skidmore
bioRxiv 2020.02.29.971093; doi: https://doi.org/10.1101/2020.02.29.971093

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